Explore studies of venom peptides.
Pardaxin possesses high antibacterial activity, and engineered variants achieved potent bacterial killing while reducing harmful effects on mammalian cells.
Oren, Z; Shai, Y · In Vitro
The pain caused by Phoneutria nigriventer venom is mediated through both peripheral and central mechanisms, involving B2 receptors, serotonin (5-HT4), glutamate (NMDA/AMPA), tachykinin (NK1/NK2), sodium channels (TTX-sensitive), acid-sensing channels (ASIC), and TRPV1 channels. Despite the venom's pain-causing nature, seven individual toxins (omega-CNTX-Pn4a, omega-CNTX-Pn2a, omega-CNTX-Pn3a, kappa-CNTX-Pn1a, U7-CNTX-Pn1a, delta-CNTX-Pn1a, Gamma-CNTX-Pn1a) and a semi-synthetic peptide (PnPP-19) have shown consistent antinociceptive (pain-relieving) properties in experimental pain models. The pain-relieving toxins work through mechanisms including calcium channel blockade, potassium channel activation, and modulation of opioid receptors.
Lauria, Pedro Santana Sales; Villarreal, Cristiane Flora; Casais-E-Silva, Luciana Lyra · Review
Venom-derived peptide toxins possess optimized pharmaceutical properties — high selectivity, potency, protease resistance, and low immunogenicity — making them ideal drug leads with several already approved.
Lazarovici, Philip · Review
Pn3a inhibits ~55% of DRG HVA calcium currents and 60-80% of Cav1.2/1.3/2.1/2.2 channels; shows additive inhibition with sub-therapeutic opioids on shared calcium channel targets.
McArthur, Jeffrey R; Munasinghe, Nehan R; Finol-Urdaneta, Rocio K; Adams, David J; Christie, Macdonald J · In Vitro
Melittin demonstrates antiviral activity against at least nine different viruses spanning multiple families, suggesting broad-spectrum potential as a venom-derived antiviral peptide.
Memariani, Hamed; Memariani, Mojtaba; Moravvej, Hamideh; Shahidi-Dadras, Mohammad · Review
The Pn3a[D8N] mutation increased NaV1.7 inhibition potency 20-fold while maintaining >100-fold selectivity over NaV1.4, NaV1.5, and NaV1.6, with confirmed analgesic activity at lower doses in vivo.
Mueller, Alexander; Dekan, Zoltan; Kaas, Quentin; Agwa, Akello J; Starobova, Hana; Alewood, Paul F; Schroeder, Christina I; Mobli, Mehdi; Deuis, Jennifer R; Vetter, Irina · Animal
Snake venom-derived peptides demonstrate validated antimicrobial and anticancer activities, with several compounds showing dual functionality against both drug-resistant bacteria and tumor cells through membrane-disrupting mechanisms.
Pérez-Peinado, Clara; Defaus, Sira; Andreu, David · Review
Ctn and Ctn[15-34] kill leukemia cells via dual membranolytic and intracellular mechanisms, with 17-fold and 7-fold tumor selectivity respectively, and protease stability up to 18-24 hours.
Pérez-Peinado, Clara; Valle, Javier; Freire, João M; Andreu, David · In Vitro
Venom-derived peptides from diverse species (bees, cone snails, sea anemones, scorpions, snakes, spiders) show potential for glycemic control, building on the proven success of exendin-4/exenatide.
Coulter-Parkhill, Aimee; McClean, Stephen; Gault, Victor A; Irwin, Nigel · Review
From 171 reviewed studies, arthropod-derived peptides from 9 animal groups demonstrated anti-inflammatory activity, primarily by decreasing pro-inflammatory cytokines in vitro and in vivo, with some also exhibiting anticancer properties.
Dos Santos, Ariane Teixeira; Cruz, Gabriela Silva; Baptista, Gandhi Rádis · Systematic Review
Multiple scorpion venom peptides have demonstrated antiviral activity against several viral families, with potential biomedical applications against HIV, hepatitis, and coronaviruses.
El Hidan, Moulay Abdelmonaim; Laaradia, Mehdi Ait; El Hiba, Omar; Draoui, Ahmed; Aimrane, Abdelmohcine; Kahime, Kholoud · Review
Snake venoms contain multiple cardiovascular-active peptide classes: PLA2, natriuretic peptides, bradykinin-potentiating peptides, CRISPs, disintegrins, fibrinolytic enzymes, and three-finger toxins, with mechanisms including vasorelaxation, anti-platelet activity, and cardioprotection.
Frangieh, Jacinthe; Rima, Mohamad; Fajloun, Ziad; Henrion, Daniel; Sabatier, Jean-Marc; Legros, Christian; Mattei, César · Review
Visabron c(4-4), a backbone cyclic octapeptide derived from viper venom disintegrin, effectively reduced EAE disease severity in mice while showing no immunogenicity or off-target toxicity.
Gilon, Chaim; Klazas, Michal; Lahiani, Adi; Schumacher-Klinger, Adi; Merzbach, Shira; Naoum, Johnny N; Ovadia, Haim; Rubin, Limor; Cornell-Kennon, Susan; Schaefer, Erik M; Katzhendler, Jehoshua; Marcinkiewicz, Cezary; Hoffman, Amnon; Lazarovici, Philip · Preclinical Animal Study
BPP-10c acts on both renin-angiotensin and kinin-kallikrein systems: inhibits ACE (reducing angiotensin II), enhances bradykinin B2 receptor effects, and increases nitric oxide — addressing the dual system disruption caused by SARS-CoV-2.
Gouda, Ahmed S; Mégarbane, Bruno · Review
KV1.3 ion channel inhibitors derived from venom peptides selectively suppress effector memory T cells involved in autoimmune diseases, with multiple medicinal chemistry approaches being pursued to optimize them as therapeutics.
Gubič, Špela; Hendrickx, Louise A; Toplak, Žan; Sterle, Maša; Peigneur, Steve; Tomašič, Tihomir; Pardo, Luis A; Tytgat, Jan; Zega, Anamarija; Mašič, Lucija P · Review
Hp1404 analog peptides showed reduced cytotoxicity, enhanced activity against MDR A. baumannii, dual membrane disruption (outer + cytoplasmic), and improved biofilm inhibition at low concentrations compared to parent peptide.
Hong, Min Ji; Kim, Min Kyung; Park, Yoonkyung · In Vitro Study
C. textile and C. miles venom subfractions activated CB1 receptor internalization, reduced pain in formalin test and nerve injury model after intrathecal injection, and showed mild to no side effects in CB tetrad assessment. Active components confirmed as peptides.
Jergova, Stanislava; Perez, Cecilia; Imperial, Julita S; Gajavelli, Shyam; Jain, Aakangsha; Abin, Adam; Olivera, Baldomero M; Sagen, Jacqueline · Preclinical Animal Study
Ring-opening metathesis polymerization (ROMP) mechanism enables controllable P22 VLP disassembly under physiological conditions (neutral pH, moderate temperature). Norbornene-conjugated VLPs disassemble upon AquaMet catalyst treatment, releasing GFP reporter cargo.
Kelly, M Patrick; Napolitano, Tanya; Anand, Prachi; Ho, Justin S K; Jabeen, Shakeela; Kuppan, Jessica; Manir, Sujoy; Holford, Mandë · In Vitro
Tachyplesin demonstrated effective anti-leishmanial activity against Leishmania donovani, the causative agent of visceral leishmaniasis, through a peptide-mediated parasite killing mechanism.
Kumar, Vivek; Chugh, Archana · In Vitro
Linear beta-defensins from snakes were most active against E. coli, M. luteus, C. freundii, and S. aureus. Shorter derived peptides (7-14 amino acids) also showed antibacterial activity against those bacteria plus K. pneumoniae. However, none of the derived peptides killed any of the four fungi tested (C. albicans, C. neoformans, T. rubrum, A. fumigatus). The key difference was the cysteine-to-serine substitution used to create the linear peptides. This suggests that the disulfide bridges formed by cysteines are essential for antifungal activity but less important for killing bacteria. Adding tryptophan (an amino acid) to the derived peptides improved their antibacterial potency. The researchers concluded that while snake beta-defensins are not the most powerful antimicrobials, they serve as useful starting templates for designing new antibiotics.
Oguiura, Nancy; Corrêa, Poliana Garcia; Rosmino, Isabella Lemos; de Souza, Ana Olívia; Pasqualoto, Kerly Fernanda Mesquita · Basic Research
One of the biggest barriers in gene therapy is the endosomal trap. Cells engulf nanoparticles carrying therapeutic genes, but the particles get stuck inside endosomes and are destroyed before they can deliver their cargo to the cell nucleus. Melittin, a 26-amino-acid peptide from bee venom, can disrupt endosomal membranes and release the trapped cargo. However, melittin is extremely toxic to mammalian cells at normal concentrations because it also destroys the outer cell membrane. Researchers have addressed this by modifying melittin's amino acid sequence to reduce its toxicity while preserving its membrane-disrupting ability. Strategies include making pH-sensitive versions that only activate inside acidic endosomes (where the gene cargo is trapped) and conjugating melittin to nanoparticle carriers so it acts locally rather than freely.
Paray, Bilal Ahamad; Ahmad, Aqeel; Khan, Javed Masood; Taufiq, Faisal; Pathan, Aslam; Malik, Ajamaluddin; Ahmed, Mohammad Z · Review
Various peptides isolated from venomous animals (spiders, scorpions, and others) can potently and selectively bind to the outer pore region of the TRPV1 ion channel — a key pain receptor. These venom peptides can either activate or inhibit TRPV1, and their specificity for this particular region of the receptor makes them valuable templates for designing new pain medications. TRPV1 is activated by multiple painful stimuli including heat, acid, and inflammatory chemicals, and contributes to both acute and chronic pain conditions. By targeting its outer pore rather than its ligand-binding site, venom peptides offer a mechanistically distinct approach to controlling pain signaling.
Hwang, Sung-Min; Jo, Youn-Yi; Cohen, Cinder Faith; Kim, Yong-Ho; Berta, Temugin; Park, Chul-Kyu · Review
NOR-1202 showed route-dependent antiepileptic effects. Direct brain injection (intracerebroventricular) protected against pilocarpine-induced generalized seizures and mortality. In the kainic acid model, it improved survival but did not prevent seizures. Systemic administration (subcutaneous or intraperitoneal) showed no antiepileptic activity, suggesting the peptide cannot cross the blood-brain barrier. In a chronic temporal lobe epilepsy model, NOR-1202 did not significantly reduce spontaneous recurrent seizures.
Quintanilha, Maria Varela Torres; Gobbo, Giovanna de Azevedo Mello; Pinheiro, Gabriela Beserra; Souza, Adolfo Carlos Barros de; Camargo, Luana Cristina; Mortari, Marcia Renata · Animal Study
Patch-clamp electrophysiology is the most reliable method for assessing peptide toxin effects on ion channels, but is underutilized in Central and South American toxinology research due to technical and infrastructure barriers.
Rojas-Palomino, Jessica; Gómez-Restrepo, Alejandro; Salinas-Restrepo, Cristian; Segura, César; Giraldo, Marco A; Calderón, Juan C · Review
Snake venoms contain a diverse arsenal of bioactive peptides and proteins that kill bacteria through multiple mechanisms: punching holes in cell membranes, enzymatically degrading microbial structures, generating oxidative stress, breaking up biofilms, and modulating the immune system. These compounds show broad-spectrum activity against drug-resistant bacteria in lab settings. The review also highlights a newer discovery — snake venom-derived extracellular vesicles (SVEVs) — tiny membrane-bound packages that protect venom compounds from degradation and improve their delivery to target sites. Advanced delivery strategies including PEGylation, liposomes, hydrogels, microneedle patches, and nanoparticles are being developed to reduce the toxicity of these venom compounds while preserving their antimicrobial potency.
Muttiah, Barathan; Hanafiah, Alfizah · Review
Neonate rattlesnake venom contained 5-7 times more potassium than adult venom, potentially enhancing the toxicity of smaller venom volumes.
Oubkeo, Crystal; Ng, Kaitlyn; Reiser, Kristofer; VanEthen, Zoe; Mackessy, Stephen P; Apawu, Aaron K · In Vitro
Intranasal AaTs-1 significantly reduced pain hypersensitivity and neuroinflammation while preventing morpho-functional alterations in spinal cord neurons and glial cells in a formalin-induced chronic pain model.
Pagano, Salvatore; Limongelli, Rebecca; Moslah, Wassim; Saada, Mohamed-Chiheb; Manzo, Iolanda; Bonsale, Roozbe; Teweldemedhin, Milena Melake; Fusco, Antimo; Guida, Francesca; Belardo, Carmela; Morace, Andrea Maria; Perrone, Michela; Ricciardi, Federica; Pierretti, Gorizio; Vastarella, Maria Giovanna; Infantino, Rosmara; Srairi-Abid, Najet; Maione, Sabatino; Palazzo, Enza; Luongo, Livio · Animal Study